Evidence for recycling of the hepatic membrane receptor for asialoglycoproteins has been obtained in freshly isolated rat liver hepatocytes. The topological distribution of the receptor in the plasma membrane has been examined. Functional binding activity is restricted to the outer surface of the membrane although the peptide chain penetrates the lipid bilayer and is exposed on the cytosolic surface. Insertion of the solubilized receptor into unilamellar lipid vesicles is accompanied by conformational changes associated with restoration of binding activity.